Q15025 (TNIP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
TNFAIP3-interacting protein 1

Alternative name(s):
A20-binding inhibitor of NF-kappa-B activation 1
Short name=ABIN-1
HIV-1 Nef-interacting protein
Nef-associated factor 1
Short name=Naf1
Nip40-1
Virion-associated nuclear shuttling protein
Short name=VAN
Short name=hVAN

Gene names

Name:	TNIP1
Synonyms:	KIAA0113, NAF1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	636 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Interacts with zinc finger protein A20/TNFAIP3 and inhibits TNF-induced NF-kappa-B-dependent gene expression by interfering with an RIP- or TRAF2-mediated transactivation signal; however, binding to A20/TNFAIP3 seems not to be required for this function By similarity. Inhibits NF-kappa-B activation by regulating A20/TNFAIP3-mediated deubiquitination of IKBKG; proposed to link A20/TNFAIP3 to ubiquitinated IKBKG. Involved in regulation of EGF-induced ERK1/ERK2 signaling pathway; blocks MAPK3/MAPK1 nuclear translocation and MAPK1-dependent transcricption. Increases cell surface CD4(T4) antigen expression. Involved in the anti-inflammatory response of macrophages and positively regulates TLR-induced activation of CEBPB. Involved in the prevention of autoimmunity; this function implicates binding to polyubiquitin. Involved in leukocyte integrin activation during inflammation; this function is mediated by association with SELPLG and dependent on phosohorylation by SRC-family kinases. Interacts with HIV-1 matrix protein and is packaged into virions and overexpression can inhibit viral replication. May regulate matrix nuclear localization, both nuclear import of PIC (Preintegration complex) and export of GAG polyprotein and viral genomic RNA during virion production. In case of infection, promotes association of IKBKG with Shigella flexneri E3 ubiquitin-protein ligase ipah9.8 p which in turn promotes polyubiquitination of IKBKG leading to its proteasome-dependent degradation and thus is perturbing NF-kappa-B activation during bacterial infection. Ref.12 Ref.13 Ref.15 Ref.18
Subunit structure	Interacts with TNFAIP3 and IKBKG; facilitates TNFAIP3-mediated de-ubiquitination of NEMO/IKBKG. Interacts with HIV-1 matrix protein. Interacts with Shigella flexneri ipah9.8; the interaction promotes polyubiquitination of IKBKG. Interacts with polyubiquitin. Interacts with MAPK1, SELPLG and PIK3CD. Interacts with IKBKG (polyubiquitinated). Interacts with IRAK1 (polyubiquitinated). Interacts with MYD88; the interaction is indicative for participation in an activated TLR-signaling complex By similarity. Ref.12 Ref.13 Ref.15 Ref.18
Subcellular location	Cytoplasm. Nucleus. Note: Shuttles between the nucleus and cytoplasm in a CRM1-dependent manner.
Tissue specificity	Ubiquitous. Strongly expressed in peripheral blood lymphocytes, spleen and skeletal muscle, and is weakly expressed in the brain.
Post-translational modification	Phosphorylation at Tyr-552 by SRC-family kinases recruits phosphoinositide-3-kinase (PI3K) PIK3CD:p85 heterodimer which results in integrin activation and leukocyte adhesion to activated endothelium during inflammation.
Sequence caution	The sequence AAB41438.1 differs from that shown. Reason: Frameshift at positions 152 and 154.

Ontologies

Keywords
Biological process	Inflammatory response
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	MyD88-dependent toll-like receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB defense response Traceable author statement Ref.1. Source: ProtInc glycoprotein biosynthetic process Inferred from direct assay Ref.1. Source: UniProtKB inflammatory response Inferred from electronic annotation. Source: UniProtKB-KW leukocyte cell-cell adhesion Inferred from mutant phenotype Ref.15. Source: UniProtKB modulation by symbiont of host I-kappaB kinase/NF-kappaB cascade Inferred from direct assay Ref.18. Source: UniProtKB negative regulation of ERK1 and ERK2 cascade Inferred from direct assay Ref.12. Source: UniProtKB negative regulation of I-kappaB kinase/NF-kappaB cascade Inferred from direct assay Ref.13. Source: UniProtKB negative regulation of viral genome replication Traceable author statement Ref.1. Source: UniProtKB positive regulation of inflammatory response Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: UniProtKB translation Traceable author statement Ref.1. Source: ProtInc
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	mitogen-activated protein kinase binding Inferred from direct assay Ref.12. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CCNG1	P51959	3	EBI-357849,EBI-3905829
GIT2	Q14161	3	EBI-357849,EBI-1046878
IKBKG	Q9Y6K9	4	EBI-357849,EBI-81279
ipaH9.8	Q8VSC3	4	EBI-357849,EBI-6125799	From a different organism.
MAGEB18	Q96M61	2	EBI-357849,EBI-741835

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q15025-1)

Also known as: Alpha;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q15025-2)

Also known as: Beta;

The sequence of this isoform differs from the canonical sequence as follows:
     627-636: SPKNDREGPQ → PADLRLPRN

Note: No experimental confirmation available.

Isoform 3 (identifier: Q15025-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-53: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 636	636	TNFAIP3-interacting protein 1		PRO_0000096691
Regions
	Region	94 – 412	319	Interacts with Nef
	Region	351 – 367	17	Interaction with Shigella flexneri ipah9.8
	Region	431 – 588	158	Required for inhibitory activity of TNF-induced NF-kappa-B activation By similarity
	Region	452 – 510	59	Ubiquitin-binding domain (UBD)
	Coiled coil	20 – 73	54	Potential
	Coiled coil	196 – 258	63	Potential
	Coiled coil	294 – 535	242	Potential
	Motif	524 – 530	7	Nuclear localization signal Potential
	Compositional bias	539 – 636	98	Pro-rich
Amino acid modifications
	Modified residue	403	1	Phosphoserine Ref.14 Ref.16 Ref.19
	Modified residue	438	1	Phosphothreonine Ref.17
	Modified residue	442	1	Phosphoserine Ref.19
	Modified residue	552	1	Phosphotyrosine Ref.15
Natural variations
	Alternative sequence	1 – 53	53	Missing in isoform 3.		VSP_045296
	Alternative sequence	627 – 636	10	SPKNDREGPQ → PADLRLPRN in isoform 2.		VSP_003913
	Natural variant	103	1	P → S. Corresponds to variant rs2303018 [ dbSNP | Ensembl ].		VAR_051453
	Natural variant	146	1	A → V. Corresponds to variant rs2233289 [ dbSNP | Ensembl ].		VAR_051454
	Natural variant	151	1	P → A. Corresponds to variant rs2233290 [ dbSNP | Ensembl ].		VAR_051455
	Natural variant	233	1	R → Q. Corresponds to variant rs2233292 [ dbSNP | Ensembl ].		VAR_051456
	Natural variant	260	1	A → V. Corresponds to variant rs2233295 [ dbSNP | Ensembl ].		VAR_051457
	Natural variant	263	1	R → W in patients with gastrointestinal diffuse large cell lymphoma. Ref.22		VAR_067965
	Natural variant	286	1	T → M in patients with gastrointestinal diffuse large cell lymphoma; somatic mutation. Ref.22		VAR_067966
	Natural variant	374	1	I → T in patients with gastrointestinal diffuse large cell lymphoma. Ref.22		VAR_067967
	Natural variant	476	1	E → K in patients with gastrointestinal diffuse large cell lymphoma; somatic mutation; loss of inhibitory activity on CARD11- and TNF-induced NF-kappa-B activation. Ref.22		VAR_067968
Experimental info
	Mutagenesis	472	1	D → N: Abolishes binding to polyubiquitin ('K-63'-linked and linear). Ref.18 Ref.21
	Mutagenesis	552	1	Y → F: Abolishes interaction with PI3K p85 regulatory subunit and abolishes interaction between SELPLG and PI3K p85 regulatory subunit. Ref.15 Ref.18
	Sequence conflict	148	1	G → D in AAH12133. Ref.9
	Sequence conflict	178	1	G → S in BAH13185. Ref.5
	Sequence conflict	299	1	A → P in AAG42154. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Alpha) [UniParc]. Last modified August 1, 1999. Version 2. Checksum: D81B96BEAD50D871	FASTA	636	71,864
	10 20 30 40 50 60 MEGRGPYRIY DPGGSVPSGE ASAAFERLVK ENSRLKEKMQ GIKMLGELLE ESQMEATRLR 70 80 90 100 110 120 QKAEELVKDN ELLPPPSPSL GSFDPLAELT GKDSNVTASP TAPACPSDKP APVQKPPSSG 130 140 150 160 170 180 TSSEFEVVTP EEQNSPESSS HANAMALGPL PREDGNLMLH LQRLETTLSV CAEEPDHGQL 190 200 210 220 230 240 FTHLGRMALE FNRLASKVHK NEQRTSILQT LCEQLRKENE ALKAKLDKGL EQRDQAAERL 250 260 270 280 290 300 REENLELKKL LMSNGNKEGA SGRPGSPKME GTGKKAVAGQ QQASVTAGKV PEVVALGAAE 310 320 330 340 350 360 KKVKMLEQQR SELLEVNKQW DQHFRSMKQQ YEQKITELRQ KLADLQKQVT DLEAEREQKQ 370 380 390 400 410 420 RDFDRKLLLA KSKIEMEETD KEQLTAEAKE LRQKVKYLQD QLSPLTRQRE YQEKEIQRLN 430 440 450 460 470 480 KALEEALSIQ TPPSSPPTAF GSPEGAGALL RKQELVTQNE LLKQQVKIFE EDFQRERSDR 490 500 510 520 530 540 ERMNEEKEEL KKQVEKLQAQ VTLSNAQLKA FKDEEKAREA LRQQKRKAKA SGERYHVEPH 550 560 570 580 590 600 PEHLCGAYPY AYPPMPAMVP HHGFEDWSQI RYPPPPMAME HPPPLPNSRL FHLPEYTWRL 610 620 630 PCGGVRNPNQ SSQVMDPPTA RPTEPESPKN DREGPQ
	Isoform 2 (Beta) [UniParc]. Checksum: FE65D2CE6E7B185B	FASTA	635	71,788
	10 20 30 40 50 60 MEGRGPYRIY DPGGSVPSGE ASAAFERLVK ENSRLKEKMQ GIKMLGELLE ESQMEATRLR 70 80 90 100 110 120 QKAEELVKDN ELLPPPSPSL GSFDPLAELT GKDSNVTASP TAPACPSDKP APVQKPPSSG 130 140 150 160 170 180 TSSEFEVVTP EEQNSPESSS HANAMALGPL PREDGNLMLH LQRLETTLSV CAEEPDHGQL 190 200 210 220 230 240 FTHLGRMALE FNRLASKVHK NEQRTSILQT LCEQLRKENE ALKAKLDKGL EQRDQAAERL 250 260 270 280 290 300 REENLELKKL LMSNGNKEGA SGRPGSPKME GTGKKAVAGQ QQASVTAGKV PEVVALGAAE 310 320 330 340 350 360 KKVKMLEQQR SELLEVNKQW DQHFRSMKQQ YEQKITELRQ KLADLQKQVT DLEAEREQKQ 370 380 390 400 410 420 RDFDRKLLLA KSKIEMEETD KEQLTAEAKE LRQKVKYLQD QLSPLTRQRE YQEKEIQRLN 430 440 450 460 470 480 KALEEALSIQ TPPSSPPTAF GSPEGAGALL RKQELVTQNE LLKQQVKIFE EDFQRERSDR 490 500 510 520 530 540 ERMNEEKEEL KKQVEKLQAQ VTLSNAQLKA FKDEEKAREA LRQQKRKAKA SGERYHVEPH 550 560 570 580 590 600 PEHLCGAYPY AYPPMPAMVP HHGFEDWSQI RYPPPPMAME HPPPLPNSRL FHLPEYTWRL 610 620 630 PCGGVRNPNQ SSQVMDPPTA RPTEPEPADL RLPRN
	Isoform 3 [UniParc]. Checksum: A97F0EB85F9F39DE	FASTA	583	66,012
	10 20 30 40 50 60 MEATRLRQKA EELVKDNELL PPPSPSLGSF DPLAELTGKD SNVTASPTAP ACPSDKPAPV 70 80 90 100 110 120 QKPPSSGTSS EFEVVTPEEQ NSPESSSHAN AMALGPLPRE DGNLMLHLQR LETTLSVCAE 130 140 150 160 170 180 EPDHGQLFTH LGRMALEFNR LASKVHKNEQ RTSILQTLCE QLRKENEALK AKLDKGLEQR 190 200 210 220 230 240 DQAAERLREE NLELKKLLMS NGNKEGASGR PGSPKMEGTG KKAVAGQQQA SVTAGKVPEV 250 260 270 280 290 300 VALGAAEKKV KMLEQQRSEL LEVNKQWDQH FRSMKQQYEQ KITELRQKLA DLQKQVTDLE 310 320 330 340 350 360 AEREQKQRDF DRKLLLAKSK IEMEETDKEQ LTAEAKELRQ KVKYLQDQLS PLTRQREYQE 370 380 390 400 410 420 KEIQRLNKAL EEALSIQTPP SSPPTAFGSP EGAGALLRKQ ELVTQNELLK QQVKIFEEDF 430 440 450 460 470 480 QRERSDRERM NEEKEELKKQ VEKLQAQVTL SNAQLKAFKD EEKAREALRQ QKRKAKASGE 490 500 510 520 530 540 RYHVEPHPEH LCGAYPYAYP PMPAMVPHHG FEDWSQIRYP PPPMAMEHPP PLPNSRLFHL 550 560 570 580 PEYTWRLPCG GVRNPNQSSQ VMDPPTARPT EPESPKNDRE GPQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and cloning of a novel cellular protein Naf1, Nef-associated factor 1, that increases cell surface CD4 expression." Fukushi M., Dixon J., Kimura T., Tsurutani N., Dixon M.J., Yamamoto N. FEBS Lett. 442:83-88(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). Tissue: Peripheral blood.
[2]	"A human nuclear shuttling protein that interacts with human immunodeficiency virus type 1 matrix is packaged into virions." Gupta K., Ott D., Hope T.J., Siliciano R.F., Boeke J.D. J. Virol. 74:11811-11824(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Leukocyte.
[3]	"Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1." Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N. DNA Res. 2:37-43(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Bone marrow.
[4]	"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones." Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T. DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION.
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[6]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Colon endothelium.
[7]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Lung.
[10]	"Transcriptional map of the Treacher Collins candidate gene region." Loftus S.K., Dixon J., Koprivnikar K., Dixon M.J., Wasmuth J.J. Genome Res. 6:26-34(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 136-636 (ISOFORM 2). Tissue: Craniofacial.
[11]	Fukushi M., Kimura T., Yamamoto N. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 94-412.
[12]	"A new ERK2 binding protein, Naf1, attenuates the EGF/ERK2 nuclear signaling." Zhang S., Fukushi M., Hashimoto S., Gao C., Huang L., Fukuyo Y., Nakajima T., Amagasa T., Enomoto S., Koike K., Miura O., Yamamoto N., Tsuchida N. Biochem. Biophys. Res. Commun. 297:17-23(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH MAPK1.
[13]	"ABIN-1 binds to NEMO/IKKgamma and co-operates with A20 in inhibiting NF-kappaB." Mauro C., Pacifico F., Lavorgna A., Mellone S., Iannetti A., Acquaviva R., Formisano S., Vito P., Leonardi A. J. Biol. Chem. 281:18482-18488(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH IKBKG AND TNFAIP3.
[14]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"P-selectin primes leukocyte integrin activation during inflammation." Wang H.B., Wang J.T., Zhang L., Geng Z.H., Xu W.L., Xu T., Huo Y., Zhu X., Plow E.F., Chen M., Geng J.G. Nat. Immunol. 8:882-892(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SELPLG AND PIK3CD, PHOSPHORYLATION AT TYR-552, MUTAGENESIS OF TYR-552.
[16]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-438, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[18]	"A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKgamma to dampen the host NF-kappaB-mediated inflammatory response." Ashida H., Kim M., Schmidt-Supprian M., Ma A., Ogawa M., Sasakawa C. Nat. Cell Biol. 12:66-73(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SHIGELLA FLEXNERI IPAH9.8, MUTAGENESIS OF 476-GLU-ARG-477.
[19]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-403 AND SER-442, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]	"Polyubiquitin binding to ABIN1 is required to prevent autoimmunity." Nanda S.K., Venigalla R.K., Ordureau A., Patterson-Kane J.C., Powell D.W., Toth R., Arthur J.S., Cohen P. J. Exp. Med. 208:1215-1228(2011) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITIN-BINDING, MUTAGENESIS OF ASP-472.
[22]	"A20, ABIN-1/2, and CARD11 mutations and their prognostic value in gastrointestinal diffuse large B-cell lymphoma." Dong G., Chanudet E., Zeng N., Appert A., Chen Y.W., Au W.Y., Hamoudi R.A., Watkins A.J., Ye H., Liu H., Gao Z., Chuang S.S., Srivastava G., Du M.Q. Clin. Cancer Res. 17:1440-1451(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS TRP-263; MET-286; THR-374 AND LYS-476.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ011895 mRNA. Translation: CAA09855.1. AJ011896 mRNA. Translation: CAA09856.1. AY012155 mRNA. Translation: AAG42154.1. D30755 mRNA. Translation: BAA06416.2. AK299975 mRNA. Translation: BAH13185.1. BX640647 mRNA. Translation: CAE45793.1. AC008641 Genomic DNA. No translation available. CH471062 Genomic DNA. Translation: EAW61690.1. BC012133 mRNA. Translation: AAH12133.1. BC014008 mRNA. Translation: AAH14008.1. U39403 mRNA. Translation: AAC99999.1. U83844 mRNA. Translation: AAB41438.1. Frameshift.
IPI	IPI00216616. IPI00783750.
RefSeq	NP_001239315.1. NM_001252386.1. NP_001239319.1. NM_001252390.1. NP_001239320.1. NM_001252391.1. NP_001239321.1. NM_001252392.1. NP_001239322.1. NM_001252393.1. NP_001245383.1. NM_001258454.1. NP_006049.3. NM_006058.4.
UniGene	Hs.355141. Hs.731557.
3D structure databases
ProteinModelPortal	Q15025.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-27577N.
IntAct	Q15025. 24 interactions.
MINT	MINT-200912.
STRING	9606.ENSP00000317891.
PTM databases
PhosphoSite	Q15025.
Polymorphism databases
DMDM	20138952.
Proteomic databases
PaxDb	Q15025.
PRIDE	Q15025.
Protocols and materials databases
DNASU	10318.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000315050; ENSP00000317891; ENSG00000145901. ENST00000389378; ENSP00000374029; ENSG00000145901. ENST00000518977; ENSP00000430971; ENSG00000145901. ENST00000520931; ENSP00000429891; ENSG00000145901. ENST00000521591; ENSP00000430760; ENSG00000145901. ENST00000522226; ENSP00000428187; ENSG00000145901. ENST00000523338; ENSP00000428243; ENSG00000145901.
GeneID	10318.
KEGG	hsa:10318.
UCSC	uc003ltg.3. human.
Organism-specific databases
CTD	10318.
GeneCards	GC05M150409.
HGNC	HGNC:16903. TNIP1.
HPA	HPA037893.
MIM	607714. gene.
neXtProt	NX_Q15025.
PharmGKB	PA128394573.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG120932.
HOGENOM	HOG000253048.
HOVERGEN	HBG019072.
InParanoid	Q15025.
OMA	PNSRLFH.
OrthoDB	EOG4ZS934.
Gene expression databases
ArrayExpress	Q15025.
Bgee	Q15025.
CleanEx	HS_NAF1. HS_TNIP1.
Genevestigator	Q15025.
GermOnline	ENSG00000145901. Homo sapiens.
Family and domain databases
ProtoNet	Search...
Other
ChiTaRS	TNIP1. human.
GenomeRNAi	10318.
NextBio	35479913.
SOURCE	Search...

Entry information

Entry name

TNIP1_HUMAN

Accession

Primary (citable) accession number: Q15025
Secondary accession number(s): B7Z699 , O76008, Q6N077, Q96EL9, Q99833, Q9H1J3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	August 1, 1999
Last modified:	May 1, 2013
This is version 122 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.